AMY2A

Mammalian protein found in Homo sapiens
AMY2A
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1B2Y, 1BSI, 1CPU, 1HNY, 1KB3, 1KBB, 1KBK, 1KGU, 1KGW, 1KGX, 1U2Y, 1U30, 1U33, 1XCW, 1XCX, 1XD0, 1XD1, 1XGZ, 1XH0, 1XH1, 1XH2, 2CPU, 2QMK, 2QV4, 3BAI, 3BAJ, 3BAK, 3BAW, 3BAX, 3BAY, 3CPU, 3IJ7, 3IJ8, 3IJ9, 3OLD, 3OLE, 3OLG, 3OLI, 4GQQ, 4GQR, 4W93, 4X9Y, 5EMY

Identifiers
AliasesAMY2A, AMY2, AMY2B, PA, amylase, alpha 2A (pancreatic), amylase alpha 2A (pancreatic), amylase alpha 2A
External IDsOMIM: 104650 MGI: 88019 HomoloGene: 20179 GeneCards: AMY2A
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for AMY2A
Genomic location for AMY2A
Band1p21.1Start103,617,427 bp[1]
End103,625,780 bp[1]
Gene location (Mouse)
Chromosome 3 (mouse)
Chr.Chromosome 3 (mouse)[2]
Chromosome 3 (mouse)
Genomic location for AMY2A
Genomic location for AMY2A
Band3 F3|3 49.35 cMStart113,349,359 bp[2]
End113,400,348 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • body of pancreas

  • islet of Langerhans

  • duodenum

  • nucleus accumbens

  • fundus

  • putamen

  • caudate nucleus

  • right lobe of liver

  • hippocampus proper

  • right coronary artery
Top expressed in
  • parotid gland

  • lacrimal gland

  • submandibular gland

  • intercostal muscle

  • left lobe of liver

  • white adipose tissue

  • subcutaneous adipose tissue

  • paraventricular nucleus of hypothalamus

  • dorsomedial hypothalamic nucleus

  • brown adipose tissue
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • chloride ion binding
  • calcium ion binding
  • catalytic activity
  • alpha-amylase activity
  • hydrolase activity
  • metal ion binding
  • hydrolase activity, acting on glycosyl bonds
  • cation binding
Cellular component
  • extracellular region
  • extracellular exosome
  • extracellular space
Biological process
  • carbohydrate catabolic process
  • polysaccharide digestion
  • metabolism
  • carbohydrate metabolic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

279

11722

Ensembl

ENSG00000243480

ENSMUSG00000074264

UniProt

P04746

P00687

RefSeq (mRNA)

NM_000699

NM_001110505
NM_007446

RefSeq (protein)

NP_000690

NP_001103975
NP_031472

Location (UCSC)Chr 1: 103.62 – 103.63 MbChr 3: 113.35 – 113.4 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Pancreatic alpha-amylase is an enzyme that in humans is encoded by the AMY2A gene.[5][6]

Amylases are secreted proteins that hydrolyze 1,4-alpha-glucoside bonds in oligosaccharides and polysaccharides, and thus catalyze the first step in digestion of dietary starch and glycogen. The human genome has a cluster of several amylase genes that are expressed at high levels in either salivary gland or pancreas. This gene encodes an amylase isoenzyme produced by the pancreas.[6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000243480 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000074264 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Groot PC, Bleeker MJ, Pronk JC, Arwert F, Mager WH, Planta RJ, Eriksson AW, Frants RR (Jul 1988). "Human pancreatic amylase is encoded by two different genes". Nucleic Acids Res. 16 (10): 4724. doi:10.1093/nar/16.10.4724. PMC 336663. PMID 3260028.
  6. ^ a b "Entrez Gene: AMY2A amylase, alpha 2A; pancreatic".

External links

See also

Further reading

  • Kaczmarek MJ, Rosenmund H (1977). "The action of human pancreatic and salivary isoamylases on starch and glycogen". Clin. Chim. Acta. 79 (1): 69–73. doi:10.1016/0009-8981(77)90462-4. PMID 890964.
  • Jacob M, Lainé J, LeBel D (1993). "Specific interactions of pancreatic amylase at acidic pH. Amylase and the major protein of the zymogen granule membrane (GP-2) bind to immobilized or polymerized amylase". Biochem. Cell Biol. 70 (10–11): 1105–14. doi:10.1139/o92-156. PMID 1284286.
  • Groot PC, Mager WH, Henriquez NV, et al. (1991). "Evolution of the human alpha-amylase multigene family through unequal, homologous, and inter- and intrachromosomal crossovers". Genomics. 8 (1): 97–105. doi:10.1016/0888-7543(90)90230-R. PMID 2081604.
  • Nishide T, Nakamura Y, Emi M, et al. (1986). "Primary structure of human salivary alpha-amylase gene". Gene. 41 (2–3): 299–304. doi:10.1016/0378-1119(86)90110-1. PMID 2423416.
  • Horii A, Emi M, Tomita N, et al. (1988). "Primary structure of human pancreatic alpha-amylase gene: its comparison with human salivary alpha-amylase gene" (PDF). Gene. 60 (1): 57–64. doi:10.1016/0378-1119(87)90213-7. hdl:11094/36665. PMID 2450054. S2CID 85098215.
  • Gumucio DL, Wiebauer K, Caldwell RM, et al. (1988). "Concerted evolution of human amylase genes". Mol. Cell. Biol. 8 (3): 1197–205. doi:10.1128/mcb.8.3.1197. PMC 363264. PMID 2452973.
  • Samuelson LC, Wiebauer K, Gumucio DL, Meisler MH (1988). "Expression of the human amylase genes: recent origin of a salivary amylase promoter from an actin pseudogene". Nucleic Acids Res. 16 (17): 8261–76. doi:10.1093/nar/16.17.8261. PMC 338557. PMID 2458567.
  • Groot PC, Bleeker MJ, Pronk JC, et al. (1989). "The human alpha-amylase multigene family consists of haplotypes with variable numbers of genes". Genomics. 5 (1): 29–42. doi:10.1016/0888-7543(89)90083-9. PMID 2788608.
  • Wise RJ, Karn RC, Larsen SH, et al. (1986). "A complementary DNA sequence that predicts a human pancreatic amylase primary structure consistent with the electrophoretic mobility of the common isozyme, Amy2 A". Mol. Biol. Med. 2 (5): 307–22. PMID 6336237.
  • Tricoli JV, Shows TB (1984). "Regional assignment of human amylase (AMY) to p22----p21 of chromosome 1". Somat. Cell Mol. Genet. 10 (2): 205–10. doi:10.1007/BF01534909. PMID 6608795. S2CID 21230969.
  • Nishide T, Emi M, Nakamura Y, Matsubara K (1984). "Corrected sequences of cDNAs for human salivary and pancreatic alpha-amylases [corrected]". Gene. 28 (2): 263–70. doi:10.1016/0378-1119(84)90265-8. PMID 6610603.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Qian M, Haser R, Buisson G, et al. (1994). "The active center of a mammalian alpha-amylase. Structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2-A resolution". Biochemistry. 33 (20): 6284–94. doi:10.1021/bi00186a031. PMID 8193143.
  • Brayer GD, Luo Y, Withers SG (1996). "The structure of human pancreatic alpha-amylase at 1.8 A resolution and comparisons with related enzymes". Protein Sci. 4 (9): 1730–42. doi:10.1002/pro.5560040908. PMC 2143216. PMID 8528071.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Rydberg EH, Sidhu G, Vo HC, et al. (1999). "Cloning, mutagenesis, and structural analysis of human pancreatic alpha-amylase expressed in Pichia pastoris". Protein Sci. 8 (3): 635–43. doi:10.1110/ps.8.3.635. PMC 2144294. PMID 10091666.
  • Brayer GD, Sidhu G, Maurus R, et al. (2000). "Subsite mapping of the human pancreatic alpha-amylase active site through structural, kinetic, and mutagenesis techniques". Biochemistry. 39 (16): 4778–91. doi:10.1021/bi9921182. PMID 10769135.
  • Aughsteen AA (2001). "A comparative immunohistochemical study on amylase localization in the rat and human exocrine pancreas". Saudi Medical Journal. 22 (5): 410–5. PMID 11376382.
  • Numao S, Maurus R, Sidhu G, et al. (2002). "Probing the role of the chloride ion in the mechanism of human pancreatic alpha-amylase". Biochemistry. 41 (1): 215–25. doi:10.1021/bi0115636. PMID 11772019.
  • v
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  • 1b2y: STRUCTURE OF HUMAN PANCREATIC ALPHA-AMYLASE IN COMPLEX WITH THE CARBOHYDRATE INHIBITOR ACARBOSE
    1b2y: STRUCTURE OF HUMAN PANCREATIC ALPHA-AMYLASE IN COMPLEX WITH THE CARBOHYDRATE INHIBITOR ACARBOSE
  • 1bsi: HUMAN PANCREATIC ALPHA-AMYLASE FROM PICHIA PASTORIS, GLYCOSYLATED PROTEIN
    1bsi: HUMAN PANCREATIC ALPHA-AMYLASE FROM PICHIA PASTORIS, GLYCOSYLATED PROTEIN
  • 1c8q: STRUCTURE SOLUTION AND REFINEMENT OF THE RECOMBINANT HUMAN SALIVARY AMYLASE
    1c8q: STRUCTURE SOLUTION AND REFINEMENT OF THE RECOMBINANT HUMAN SALIVARY AMYLASE
  • 1cpu: SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT
    1cpu: SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT
  • 1hny: The structure of human pancreatic alpha-amylase at 1.8 angstroms resolution and comparisons with related enzymes
    1hny: The structure of human pancreatic alpha-amylase at 1.8 angstroms resolution and comparisons with related enzymes
  • 1jxj: Role of mobile loop in the mechanism of human salivary amylase
    1jxj: Role of mobile loop in the mechanism of human salivary amylase
  • 1jxk: Role of the mobile loop in the mechanism of human salivary amylase
    1jxk: Role of the mobile loop in the mechanism of human salivary amylase
  • 1kb3: Three Dimensional Structure Analysis of the R195A Variant of Human Pancreatic Alpha Amylase
    1kb3: Three Dimensional Structure Analysis of the R195A Variant of Human Pancreatic Alpha Amylase
  • 1kbb: Mechanistic Analyses of Catalysis in Human Pancreatic alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids
    1kbb: Mechanistic Analyses of Catalysis in Human Pancreatic alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids
  • 1kbk: Mechanistic Analyses of Catalysis in Human Pancreatic Alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids
    1kbk: Mechanistic Analyses of Catalysis in Human Pancreatic Alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids
  • 1kgu: THREE DIMENSIONAL STRUCTURE ANALYSIS OF THE R337A VARIANT OF HUMAN PANCREATIC ALPHA-AMYLASE
    1kgu: THREE DIMENSIONAL STRUCTURE ANALYSIS OF THE R337A VARIANT OF HUMAN PANCREATIC ALPHA-AMYLASE
  • 1kgw: THREE DIMENSIONAL STRUCTURE ANALYSIS OF THE R337Q VARIANT OF HUMAN PANCREATIC ALPHA-MYLASE
    1kgw: THREE DIMENSIONAL STRUCTURE ANALYSIS OF THE R337Q VARIANT OF HUMAN PANCREATIC ALPHA-MYLASE
  • 1kgx: Three Dimensional Structure Analysis of the R195Q Variant of Human Pancreatic Alpha Amylase
    1kgx: Three Dimensional Structure Analysis of the R195Q Variant of Human Pancreatic Alpha Amylase
  • 1mfu: Probing the role of a mobile loop in human salivary amylase: Structural studies on the loop-deleted mutant
    1mfu: Probing the role of a mobile loop in human salivary amylase: Structural studies on the loop-deleted mutant
  • 1mfv: Probing the role of a mobile loop in human slaivary amylase: Structural studies on the loop-deleted enzyme
    1mfv: Probing the role of a mobile loop in human slaivary amylase: Structural studies on the loop-deleted enzyme
  • 1nm9: Crystal structure of recombinant human salivary amylase mutant W58A
    1nm9: Crystal structure of recombinant human salivary amylase mutant W58A
  • 1q4n: Structural studies of Phe256Trp of human salivary alpha-amylase: implications for the role of a conserved water molecule and its associated chain in enzyme activity
    1q4n: Structural studies of Phe256Trp of human salivary alpha-amylase: implications for the role of a conserved water molecule and its associated chain in enzyme activity
  • 1smd: HUMAN SALIVARY AMYLASE
    1smd: HUMAN SALIVARY AMYLASE
  • 1u2y: In situ extension as an approach for identifying novel alpha-amylase inhibitors, structure containing D-gluconhydroximo-1,5-lactam
    1u2y: In situ extension as an approach for identifying novel alpha-amylase inhibitors, structure containing D-gluconhydroximo-1,5-lactam
  • 1u30: In situ extension as an approach for identifying novel alpha-amylase inhibitors, structure containing maltosyl-alpha (1,4)-D-gluconhydroximo-1,5-lactam
    1u30: In situ extension as an approach for identifying novel alpha-amylase inhibitors, structure containing maltosyl-alpha (1,4)-D-gluconhydroximo-1,5-lactam
  • 1u33: In situ extension as an approach for identifying novel alpha-amylase inhibitors
    1u33: In situ extension as an approach for identifying novel alpha-amylase inhibitors
  • 1xcw: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts
    1xcw: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts
  • 1xcx: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts
    1xcx: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts
  • 1xd0: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts
    1xd0: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts
  • 1xd1: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts
    1xd1: Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts
  • 1xgz: Structure of the N298S variant of human pancreatic alpha-amylase
    1xgz: Structure of the N298S variant of human pancreatic alpha-amylase
  • 1xh0: Structure of the N298S variant of human pancreatic alpha-amylase complexed with acarbose
    1xh0: Structure of the N298S variant of human pancreatic alpha-amylase complexed with acarbose
  • 1xh1: Structure of the N298S variant of human pancreatic alpha-amylase complexed with chloride
    1xh1: Structure of the N298S variant of human pancreatic alpha-amylase complexed with chloride
  • 1xh2: Structure of the N298S variant of human pancreatic alpha-amylase complexed with chloride and acarbose
    1xh2: Structure of the N298S variant of human pancreatic alpha-amylase complexed with chloride and acarbose
  • 1xv8: Crystal Structure of Human Salivary Alpha-Amylase Dimer
    1xv8: Crystal Structure of Human Salivary Alpha-Amylase Dimer
  • 1z32: Structure-function relationships in human salivary alpha-amylase: Role of aromatic residues
    1z32: Structure-function relationships in human salivary alpha-amylase: Role of aromatic residues
  • 2cpu: SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT
    2cpu: SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT
  • 3cpu: SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT
    3cpu: SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT


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